Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Tilted peptides: a motif for membrane destabilization (hypothesis).

R Brasseur1

  • 1Centre de Biophysique Moléculaire Numérique, Faculté Universitaire des Sciences Agronomiques de Gembloux, Belgium. brasseur.r@fsagx.ac.be

Molecular Membrane Biology
|May 29, 2000
PubMed
Summary

Cellular processes rely on disrupting molecular interfaces. Newly discovered "tilted peptides" possess unique hydrophobicity, enabling them to disrupt these interfaces, suggesting a key role in cell life dynamics.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Study of the specific lipid binding properties of Abeta 11-22 fragment at endosomal pH.

Langmuir : the ACS journal of surfaces and colloids·2009
Same author

The "Tilted Peptide Theory" links membrane insertion properties and fusogenicity of viral fusion peptides.

Protein and peptide letters·2009
Same author

Study of Thermomyces lanuginosa lipase in the presence of tributyrylglycerol and water.

Biophysical journal·2009
Same author

Genomic location of the bovine growth hormone secretagogue receptor (GHSR) gene and investigation of genetic polymorphism.

Animal biotechnology·2009
Same author

Relationships between the orientation and the structural properties of peptides and their membrane interactions.

Biochimica et biophysica acta·2008
Same author

Tilted peptides: a structural motif involved in protein membrane insertion?

Journal of peptide science : an official publication of the European Peptide Society·2007

Area of Science:

  • Molecular biology
  • Biophysics

Background:

  • Cellular functions like protein folding and membrane fusion require disruption of hydrophilic/hydrophobic interfaces.
  • Amphipathic systems, including membranes and proteins, are central to these processes.

Purpose of the Study:

  • To introduce and define "tilted peptides" or "oblique peptides" as novel protein fragments.
  • To explain the mechanism by which these peptides disrupt hydrophobic interfaces.
  • To hypothesize their widespread involvement in essential cellular dynamics.

Main Methods:

  • Review of existing literature on protein structure and function.
  • Analysis of peptide hydrophobicity distribution.
  • Hypothetical modeling of peptide-interface interactions.

Related Experiment Videos

Main Results:

  • Tilted peptides exhibit a unique hydrophobic distribution enabling interface disruption.
  • Evidence suggests these peptides are present in numerous proteins.
  • A method for detecting tilted peptides is proposed.

Conclusions:

  • Tilted peptides represent a significant discovery in understanding molecular interface dynamics.
  • Their ability to disrupt hydrophobic interfaces points to a crucial role in cellular processes.
  • Further research is warranted to explore their functions in cell life.